Glucose signaling, AtRGS1 and plant autophagy

Yue, Jiao; Lei, Wenxue; Xu, Wendao; Chen, Wenli

doi:10.1080/15592324.2019.1607465

Cited by 10 publications

(5 citation statements)

References 30 publications

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“…The asparagine synthetase 2 mutant exhibits low salt stress tolerance [ 81 ] and the amino acid is imbedded into a signaling network involved in stress resistance in Arabidopsis [ 82 , 83 ]. Glucose is an important regulator of plant defense, e.g., by controlling the interaction and phosphorylation of BRI1 and BAK1 [ 84 ]. Also, the phytohormone ABA is a well-investigated abiotic stress hormone [ 85 ].…”

Section: Discussionmentioning

confidence: 99%

Cellooligomer/CELLOOLIGOMER RECEPTOR KINASE1 Signaling Exhibits Crosstalk with PAMP-Triggered Immune Responses and Sugar Metabolism in Arabidopsis Roots

Gandhi,

Reichelt,

Furch

et al. 2024

IJMS

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The degradation of cellulose generates cellooligomers, which function as damage-associated molecular patterns and activate immune and cell wall repair responses via the CELLOOLIGOMER RECEPTOR KINASE1 (CORK1). The most active cellooligomer for the induction of downstream responses is cellotriose, while cellobiose is around 100 times less effective. These short-chain cellooligomers are also metabolized after uptake into the cells. In this study, we demonstrate that CORK1 is mainly expressed in the vascular tissue of the upper, fully developed part of the roots. Cellooligomer/CORK1-induced responses interfere with chitin-triggered immune responses and are influenced by BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED RECEPTOR KINASE1 and the receptor kinase FERONIA. The pathway also controls sugar transporter and metabolism genes and the phosphorylation state of these proteins. Furthermore, cellotriose-induced ROS production and WRKY30/40 expression are controlled by the sugar transporters SUCROSE-PROTON SYMPORTER1, SUGARS WILL EVENTUALLY BE EXPORTED TRANSPORTER11 (SWEET11), and SWEET12. Our data demonstrate that cellooligomer/CORK1 signaling is integrated into the pattern recognition receptor network and coupled to the primary sugar metabolism in Arabidopsis roots.

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Section: Discussionmentioning

confidence: 99%

Cellooligomer/CELLOOLIGOMER RECEPTOR KINASE1 Signaling Exhibits Crosstalk with PAMP-Triggered Immune Responses and Sugar Metabolism in Arabidopsis Roots

Gandhi,

Reichelt,

Furch

et al. 2024

IJMS

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“…Plant Gα proteins are typically self-activated; for instance, RGS1 interacts with Gα and maintains the G-protein complex in its inactive state via its GAP activity (Pandey, 2019). In addition, Jiao et al reported that AtRGS1 increased the autophagosomes formation and autophagic flux through interaction with AtATG8a in response to D-glucose starvation (Jiao et al, 2019a; Jiao et al, 2019b). Combining these results, we hypothesized that AtGPA1 inhibited nitrate recycling through AtATG8a under low-nitrate conditions.…”

Section: Discussionmentioning

confidence: 99%

Heterotrimeric G protein α subunit (GPA1) regulates the response to low-nitrogen stress in Arabidopsis by interacting with AtNRT1.4 and AtATG8a

Luo

et al. 2022

Preprint

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Efficient nitrogen absorption and utilization are important factors for higher plants to increase yield and reduce eutrophication (caused by excessive use of nitrogen fertilizers). Heterotrimeric G proteins participate in the pathway regulating nitrogen absorption and utilization in plants. However, the regulatory mechanism remains largely obscured. In this study, our results revealed that mutant gpa1-4 was tolerant to low-nitrogen stress in Arabidopsis. AtGPA1 was shown to directly interact with a nitrate transporter (AtNRT1.4) and a key autophagy-related protein (AtATG8a) on the plasma membrane. GUS staining and subcellular localization showed that AtGPA1 and AtNRT1.4 were co-expressed in roots and leaf veins and on the plasma membrane. Under low-nitrate conditions, the single mutant gpa1-4 and NRT1.4RNAi plants (AtNRT1.4RNA interference plants) and the double mutant NRT1.4RNAi/gpa1-4 plants (AtNRT1.4RNA interference plants on a gpa1-4 background) were healthier than the wild type plants. Moreover, the phenotype of the double mutant NRT1.4RNAi/gpa1-4 plants was closer to that of the NRT1.4RNAi plants compared to that of the gpa1-4 mutants. The results of the nitrate efflux rate assay in roots were consistent with the phenotypic changes under low-nitrogen conditions. These results indicated that AtGPA1 is an upstream factor that regulated the response to low-nitrogen stress through interaction with AtNRT1.4. In addition, we found that transgenic plants overexpressing AtATG8a were more tolerant to low-nitrogen stress, and their phenotype was similar to that of gpa1-4 mutants and double mutant ATG8aOX/gpa1-4 plants. Our findings may provide a new model for improving nitrogen-use efficiency through genetical modification to boost crop yields.

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“…It has been demonstrated that AtRGS1 protein level is sensitive to glucose, and D-glucose could accelerate the association between AtRGS1 and GPA1 (Johnston et al ., 2007). AtRGS-related G-protein coupled glucose signal transduction pathway has been proved to be one of the three major sugar signaling pathways in plants (Jiao et al ., 2019a). After AtRGS1 binds to GPA1, the dissociative Gβγ heterodimer recruits AtWNK8 to phosphorylate AtRGS1.…”

Section: Introductionmentioning

confidence: 99%

ArabidopsisORP2A positively regulates glucose signaling by interacting with AtRGS1 and promoting AtRGS1 degradation

Zou

Liu

et al. 2022

Preprint

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Heterotrimeric GTP-binding proteins are a group of regulators essential for signal transmission into cells. AtRGS1 with intrinsic GTPase-accelerating protein activity could suppress G protein and glucose signal transduction in Arabidopsis. However, how AtRGS1 activity is regulated is currently poor understood. Here we identified a knockout mutant orp2a-1 which shows phenotypes similar to agb1-2. With overexpression of ORP2A, transgenic lines display short hypocotyl, hypersensitivity to sugar and lower intracellular AtRGS1 level than control. Consistently, ORP2A shows interaction with AtRGS1 in vitro and vivo. Tissue specificity of ORP2A with two alternative protein forms imply its functions in organ size and shape controlling. Bioinformatic data and phenotypes of orp2a-1, agb1-2 and double mutant reveal genetic interactions in the regulation of G protein signaling and sugar response between ORP2A and Gβ. Both alternative splicing forms of ORP2A locate in the ER, PM and EPCS, and interact with VAP27-1 mediated by a FFAT-like motif in vivo and vitro. ORP2A also displays differential phosphatidyl phosphoinositide binding activity mediated by its PH domain in vitro. Taken together, it is suggested that Arabidopsis membrane protein ORP2A interacts with AtRGS1 and VAP27-1 to positively regulate G protein and sugar signaling by facilitating AtRGS1 degradation.

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Glucose signaling, AtRGS1 and plant autophagy

Cited by 10 publications

References 30 publications

Cellooligomer/CELLOOLIGOMER RECEPTOR KINASE1 Signaling Exhibits Crosstalk with PAMP-Triggered Immune Responses and Sugar Metabolism in Arabidopsis Roots

Cellooligomer/CELLOOLIGOMER RECEPTOR KINASE1 Signaling Exhibits Crosstalk with PAMP-Triggered Immune Responses and Sugar Metabolism in Arabidopsis Roots

Heterotrimeric G protein α subunit (GPA1) regulates the response to low-nitrogen stress in Arabidopsis by interacting with AtNRT1.4 and AtATG8a

ArabidopsisORP2A positively regulates glucose signaling by interacting with AtRGS1 and promoting AtRGS1 degradation

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